dsRNAbindende

dsRNA-binding proteins, often abbreviated dsRBPs, are a diverse group of proteins that recognize double-stranded RNA (dsRNA) through one or more dsRNA-binding motifs (dsRBMs). They participate in a wide range of cellular processes, including RNA interference, innate immune sensing, RNA editing, splicing, localization, and translational regulation. Their ability to bind dsRNA is typically sequence-independent and relies on the A-form geometry of dsRNA.

Most dsRBPs contain one or more dsRNA-binding motifs, each about 65–70 amino acids in length. When present in tandem, multiple dsRBMs enable cooperative and high-affinity binding to longer dsRNA molecules and allow the protein to bridge or stabilize RNA structures. Some dsRBPs also harbor additional domains that mediate interactions with other proteins or RNA-processing enzymes, guiding downstream pathways.

Functional roles of dsRBPs vary by organism and context. In RNA interference pathways, dsRBPs assist in processing long dsRNA into small interfering RNAs (siRNAs) and loading them into effector complexes. In RNA editing, adenosine deaminases acting on RNA (ADARs) bind dsRNA substrates to catalyze A-to-I changes. In innate immunity, sensors such as RIG-I and MDA5 recognize viral dsRNA and trigger antiviral signaling. Other dsRBPs function as regulators of mRNA localization, stability, or translation, exemplified by Staufen proteins and plant DRB family members that partner with Dicer in small RNA pathways.

Across eukaryotes, dsRBPs are integral to post-transcriptional gene regulation and defense against pathogens. Variants in dsRBM-containing proteins can impact RNA metabolism and cellular responses, highlighting the importance of dsRNA recognition in biology.